CTDSL_HUMAN - dbPTM
CTDSL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTDSL_HUMAN
UniProt AC O15194
Protein Name CTD small phosphatase-like protein
Gene Name CTDSPL
Organism Homo sapiens (Human).
Sequence Length 276
Subcellular Localization Nucleus.
Protein Description Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation..
Protein Sequence MDGPAIITQVTNPKEDEGRLPGAGEKASQCNVSLKKQRSRSILSSFFCCFRDYNVEAPPPSSPSVLPPLVEENGGLQKGDQRQVIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSREDDVYSMLHRLCNR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
28PhosphorylationPGAGEKASQCNVSLK
CCCCCCHHHCCCCCC		46.4629496963
33PhosphorylationKASQCNVSLKKQRSR
CHHHCCCCCCHHHHH		22.0823401153
61PhosphorylationNVEAPPPSSPSVLPP
CCCCCCCCCCCCCCC		61.7328555341
89PhosphorylationRQVIPIPSPPAKYLL
CCEECCCCCCHHHCC		44.2129496963
93UbiquitinationPIPSPPAKYLLPEVT
CCCCCCHHHCCCEEE		42.05-
94PhosphorylationIPSPPAKYLLPEVTV
CCCCCHHHCCCEEEE		18.64-
196PhosphorylationRARLFRESCVFHRGN
HHHHHHHHCEEECCC		16.0124719451
204PhosphorylationCVFHRGNYVKDLSRL
CEEECCCHHHHHHHH		16.2324719451
267PhosphorylationLSREDDVYSMLHRLC
CCCHHHHHHHHHHHH		8.7128796482
268PhosphorylationSREDDVYSMLHRLCN
CCHHHHHHHHHHHHC		18.0823401153
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CTDSL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTDSL_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CTDSL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNAI1_HUMANSNAI1physical
19004823
CED12_CAEELced-12physical
14645848
CDCA3_HUMANCDCA3physical
27880917
TBCD4_HUMANTBC1D4physical
27880917
ARVC_HUMANARVCFphysical
27880917
CADM1_HUMANCADM1physical
27880917
RFTN1_HUMANRFTN1physical
27880917
PACS1_HUMANPACS1physical
27880917
DAB2P_HUMANDAB2IPphysical
27880917
RHG39_HUMANARHGAP39physical
27880917
CD44_HUMANCD44physical
27880917
MRP1_HUMANABCC1physical
27880917
AT2B4_HUMANATP2B4physical
27880917
NOTC1_HUMANNOTCH1physical
27880917
NECT2_HUMANPVRL2physical
27880917
MUC18_HUMANMCAMphysical
27880917
ITA5_HUMANITGA5physical
27880917
UBP31_HUMANUSP31physical
27880917
C2C4C_HUMANC2CD4Cphysical
27880917
TB10B_HUMANTBC1D10Bphysical
27880917
TIAM1_HUMANTIAM1physical
27880917
ITA6_HUMANITGA6physical
27880917
KIRR1_HUMANKIRRELphysical
27880917
SPTN2_HUMANSPTBN2physical
27880917
NEB1_HUMANPPP1R9Aphysical
27880917
BORG5_HUMANCDC42EP1physical
27880917
TMEM2_HUMANTMEM2physical
27880917
CAHD1_HUMANCACHD1physical
27880917
MICA3_HUMANMICAL3physical
27880917
ANK3_HUMANANK3physical
27880917
FMN2_HUMANFMN2physical
27880917
ROBO1_HUMANROBO1physical
27880917
MPZL1_HUMANMPZL1physical
27880917
ADDB_HUMANADD2physical
27880917
PALM2_HUMANPALM2physical
27880917
NUMBL_HUMANNUMBLphysical
27880917
AKAP5_HUMANAKAP5physical
27880917
ZNT1_HUMANSLC30A1physical
27880917
K1549_HUMANKIAA1549physical
27880917
CTNA1_HUMANCTNNA1physical
27880917
FLVC1_HUMANFLVCR1physical
27880917
S29A1_HUMANSLC29A1physical
27880917
CXAR_HUMANCXADRphysical
27880917
F171B_HUMANFAM171Bphysical
27880917
TTC7B_HUMANTTC7Bphysical
27880917
PCDH7_HUMANPCDH7physical
27880917
MALD2_HUMANMARVELD2physical
27880917
MERL_HUMANNF2physical
27880917
S39A6_HUMANSLC39A6physical
27880917
BASP1_HUMANBASP1physical
27880917
CNNM3_HUMANCNNM3physical
27880917
S39AA_HUMANSLC39A10physical
27880917
CLCN7_HUMANCLCN7physical
27880917
GRIN3_HUMANGPRIN3physical
27880917
ESYT2_HUMANESYT2physical
27880917
F1711_HUMANFAM171A1physical
27880917
AGRL2_HUMANLPHN2physical
27880917
RELL1_HUMANRELL1physical
27880917
S12A7_HUMANSLC12A7physical
27880917
NUMB_HUMANNUMBphysical
27880917
CEP89_HUMANCEP89physical
27880917
S12A2_HUMANSLC12A2physical
27880917
CTND1_HUMANCTNND1physical
27880917
DTNA_HUMANDTNAphysical
27880917
CCDC8_HUMANCCDC8physical
27880917
S38A1_HUMANSLC38A1physical
27880917
ZO1_HUMANTJP1physical
27880917
ZDHC5_HUMANZDHHC5physical
27880917
PALM_HUMANPALMphysical
27880917
EGFR_HUMANEGFRphysical
27880917
PTN14_HUMANPTPN14physical
27880917
TULP3_HUMANTULP3physical
27880917
NIBL1_HUMANFAM129Bphysical
27880917
GRIN1_HUMANGPRIN1physical
27880917
HS12A_HUMANHSPA12Aphysical
27880917
AT2B1_HUMANATP2B1physical
27880917
EFR3B_HUMANEFR3Bphysical
27880917
4F2_HUMANSLC3A2physical
27880917
AR13B_HUMANARL13Bphysical
27880917
PSD3_HUMANPSD3physical
27880917
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTDSL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY.

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